ENTRY map04130 Pathway NAME SNARE interactions in vesicular transport CLASS Genetic Information Processing; Folding, sorting and degradation PATHWAY_MAP map04130 SNARE interactions in vesicular transport REFERENCE PMID:16882042 AUTHORS Yoshizawa AC, Kawashima S, Okuda S, Fujita M, Itoh M, Moriya Y, Hattori M, Kanehisa M TITLE Extracting sequence motifs and the phylogenetic features of SNARE-dependent membrane traffic. JOURNAL Traffic 7:1104-18 (2006) DOI:10.1111/j.1600-0854.2006.00451.x REFERENCE PMID:10839363 AUTHORS Scales SJ, Chen YA, Yoo BY, Patel SM, Doung YC, Scheller RH. TITLE SNAREs contribute to the specificity of membrane fusion. JOURNAL Neuron 26:457-64 (2000) DOI:10.1016/S0896-6273(00)81177-0 REFERENCE PMID:11737951 AUTHORS Teng FY, Wang Y, Tang BL. TITLE The syntaxins. JOURNAL Genome Biol 2:REVIEWS3012 (2001) DOI:10.1186/gb-2001-2-11-reviews3012 REFERENCE PMID:11115874 AUTHORS Sanderfoot AA, Assaad FF, Raikhel NV. TITLE The Arabidopsis genome. An abundance of soluble N-ethylmaleimide-sensitive factor adaptor protein receptors. JOURNAL Plant Physiol 124:1558-69 (2000) DOI:10.1104/pp.124.4.1558 REFERENCE PMID:15342965 AUTHORS Uemura T, Ueda T, Ohniwa RL, Nakano A, Takeyasu K, Sato MH. TITLE Systematic analysis of SNARE molecules in Arabidopsis: dissection of the post-Golgi network in plant cells. JOURNAL Cell Struct Funct 29:49-65 (2004) DOI:10.1247/csf.29.49 REFERENCE PMID:10872468 AUTHORS Jahn R, Sudhof TC. TITLE Membrane fusion and exocytosis. JOURNAL Annu Rev Biochem 68:863-911 (1999) DOI:10.1146/annurev.biochem.68.1.863 REFERENCE PMID:11306253 AUTHORS Pelham HR. TITLE SNAREs and the specificity of membrane fusion. JOURNAL Trends Cell Biol 11:99-101 (2001) DOI:10.1016/S0962-8924(01)01929-8 REFERENCE PMID:11104523 AUTHORS Armstrong J TITLE Membrane traffic between genomes. JOURNAL Genome Biol 1:REVIEWS104 (2000) DOI:10.1186/gb-2000-1-1-reviews104 REFERENCE PMID:11237004 AUTHORS Bock JB, Matern HT, Peden AA, Scheller RH. TITLE A genomic perspective on membrane compartment organization. JOURNAL Nature 409:839-41 (2001) DOI:10.1038/35057024 REFERENCE PMID:11252968 AUTHORS Chen YA, Scheller RH. TITLE SNARE-mediated membrane fusion. JOURNAL Nat Rev Mol Cell Biol 2:98-106 (2001) DOI:10.1038/35052017 REFERENCE PMID:9763449 AUTHORS Seron K, Tieaho V, Prescianotto-Baschong C, Aust T, Blondel MO, Guillaud P, Devilliers G, Rossanese OW, Glick BS, Riezman H, Keranen S, Haguenauer-Tsapis R. TITLE A yeast t-SNARE involved in endocytosis. JOURNAL Mol Biol Cell 9:2873-89 (1998) DOI:10.1091/mbc.9.10.2873 REFERENCE PMID:10213783 AUTHORS Sanderfoot AA, Raikhel NV. TITLE The specificity of vesicle trafficking: coat proteins and SNAREs. JOURNAL Plant Cell 11:629-42 (1999) DOI:10.1105/tpc.11.4.629 REFERENCE PMID:9565594 AUTHORS Abeliovich H, Grote E, Novick P, Ferro-Novick S. TITLE Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic structures. JOURNAL J Biol Chem 273:11719-27 (1998) DOI:10.1074/jbc.273.19.11719 REFERENCE PMID:9553086 AUTHORS Advani RJ, Bae HR, Bock JB, Chao DS, Doung YC, Prekeris R, Yoo JS, Scheller RH. TITLE Seven novel mammalian SNARE proteins localize to distinct membrane compartments. JOURNAL J Biol Chem 273:10317-24 (1998) DOI:10.1074/jbc.273.17.10317 REFERENCE PMID:10459012 AUTHORS Advani RJ, Yang B, Prekeris R, Lee KC, Klumperman J, Scheller RH. TITLE VAMP-7 mediates vesicular transport from endosomes to lysosomes. JOURNAL J Cell Biol 146:765-76 (1999) DOI:10.1083/jcb.146.4.765 REFERENCE PMID:12893879 AUTHORS Burri L, Varlamov O, Doege CA, Hofmann K, Beilharz T, Rothman JE, Sollner TH, Lithgow T. TITLE A SNARE required for retrograde transport to the endoplasmic reticulum. JOURNAL Proc Natl Acad Sci U S A 100:9873-7 (2003) DOI:10.1073/pnas.1734000100 REFERENCE PMID:10085287 AUTHORS Chao DS, Hay JC, Winnick S, Prekeris R, Klumperman J, Scheller RH. TITLE SNARE membrane trafficking dynamics in vivo. JOURNAL J Cell Biol 144:869-81 (1999) DOI:10.1083/jcb.144.5.869 REFERENCE PMID:10397773 AUTHORS Coe JG, Lim AC, Xu J, Hong W. TITLE A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae. JOURNAL Mol Biol Cell 10:2407-23 (1999) DOI:10.1091/mbc.10.7.2407 REFERENCE PMID:11445562 AUTHORS Dilcher M, Kohler B, von Mollard GF. TITLE Genetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6. JOURNAL J Biol Chem 276:34537-44 (2001) DOI:10.1074/jbc.M101551200 REFERENCE PMID:12853481 AUTHORS Dilcher M, Veith B, Chidambaram S, Hartmann E, Schmitt HD, Fischer von Mollard G. TITLE Use1p is a yeast SNARE protein required for retrograde traffic to the ER. JOURNAL EMBO J 22:3664-74 (2003) DOI:10.1093/emboj/cdg339 REFERENCE PMID:9446565 AUTHORS Fischer von Mollard G, Stevens TH. TITLE A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways. JOURNAL J Biol Chem 273:2624-30 (1998) DOI:10.1074/jbc.273.5.2624 REFERENCE PMID:10359592 AUTHORS Fischer von Mollard G, Stevens TH. TITLE The Saccharomyces cerevisiae v-SNARE Vti1p is required for multiple membrane transport pathways to the vacuole. JOURNAL Mol Biol Cell 10:1719-32 (1999) DOI:10.1091/mbc.10.6.1719 REFERENCE PMID:9614185 AUTHORS Galli T, Zahraoui A, Vaidyanathan VV, Raposo G, Tian JM, Karin M, Niemann H, Louvard D. TITLE A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells. JOURNAL Mol Biol Cell 9:1437-48 (1998) DOI:10.1091/mbc.9.6.1437 REFERENCE PMID:11208059 AUTHORS Gerrard SR, Mecklem AB, Stevens TH. TITLE The yeast endosomal t-SNARE, Pep12p, functions in the absence of its transmembrane domain. JOURNAL Traffic 1:45-55 (2000) DOI:10.1034/j.1600-0854.2000.010108.x REFERENCE PMID:10379359 AUTHORS Gerst JE. TITLE SNAREs and SNARE regulators in membrane fusion and exocytosis. JOURNAL Cell Mol Life Sci 55:707-34 (1999) DOI:10.1007/s000180050328 REFERENCE PMID:11029060 AUTHORS Gurunathan S, Chapman-Shimshoni D, Trajkovic S, Gerst JE. TITLE Yeast exocytic v-SNAREs confer endocytosis. JOURNAL Mol Biol Cell 11:3629-43 (2000) DOI:10.1091/mbc.11.10.3629 REFERENCE PMID:10788491 AUTHORS Hatsuzawa K, Hirose H, Tani K, Yamamoto A, Scheller RH, Tagaya M. TITLE Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking. JOURNAL J Biol Chem 275:13713-20 (2000) DOI:10.1074/jbc.275.18.13713 REFERENCE PMID:8621431 AUTHORS Hay JC, Hirling H, Scheller RH. TITLE Mammalian vesicle trafficking proteins of the endoplasmic reticulum and Golgi apparatus. JOURNAL J Biol Chem 271:5671-9 (1996) DOI:10.1074/jbc.271.10.5671 REFERENCE PMID:9647643 AUTHORS Hay JC, Klumperman J, Oorschot V, Steegmaier M, Kuo CS, Scheller RH. TITLE Localization, dynamics, and protein interactions reveal distinct roles for ER and Golgi SNAREs. JOURNAL J Cell Biol 141:1489-502 (1998) DOI:10.1083/jcb.141.7.1489 REFERENCE PMID:9427746 AUTHORS Holthuis JC, Nichols BJ, Dhruvakumar S, Pelham HR. TITLE Two syntaxin homologues in the TGN/endosomal system of yeast. JOURNAL EMBO J 17:113-26 (1998) DOI:10.1093/emboj/17.1.113 REFERENCE PMID:9843576 AUTHORS Holthuis JC, Nichols BJ, Pelham HR. TITLE The syntaxin Tlg1p mediates trafficking of chitin synthase III to polarized growth sites in yeast. JOURNAL Mol Biol Cell 9:3383-97 (1998) DOI:10.1091/mbc.9.12.3383 REFERENCE PMID:12600315 AUTHORS Jahn R, Lang T, Sudhof TC. TITLE Membrane fusion. JOURNAL Cell 112:519-33 (2003) DOI:10.1016/S0092-8674(03)00112-0 REFERENCE PMID:10097106 AUTHORS Lafont F, Verkade P, Galli T, Wimmer C, Louvard D, Simons K. TITLE Raft association of SNAP receptors acting in apical trafficking in Madin-Darby canine kidney cells. JOURNAL Proc Natl Acad Sci U S A 96:3734-8 (1999) DOI:10.1073/pnas.96.7.3734 REFERENCE PMID:9214619 AUTHORS Lewis MJ, Rayner JC, Pelham HR. TITLE A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum. JOURNAL EMBO J 16:3017-24 (1997) DOI:10.1093/emboj/16.11.3017 REFERENCE PMID:9647644 AUTHORS Low SH, Chapin SJ, Wimmer C, Whiteheart SW, Komuves LG, Mostov KE, Weimbs T. TITLE The SNARE machinery is involved in apical plasma membrane trafficking in MDCK cells. JOURNAL J Cell Biol 141:1503-13 (1998) DOI:10.1083/jcb.141.7.1503 REFERENCE PMID:9452464 AUTHORS Low SH, Roche PA, Anderson HA, van Ijzendoorn SC, Zhang M, Mostov KE, Weimbs T. TITLE Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells. JOURNAL J Biol Chem 273:3422-30 (1998) DOI:10.1074/jbc.273.6.3422 REFERENCE PMID:12669082 AUTHORS Mostov K, Su T, ter Beest M. TITLE Polarized epithelial membrane traffic: conservation and plasticity. JOURNAL Nat Cell Biol 5:287-93 (2003) DOI:10.1038/ncb0403-287 REFERENCE PMID:10873817 AUTHORS Mostov KE, Verges M, Altschuler Y. TITLE Membrane traffic in polarized epithelial cells. JOURNAL Curr Opin Cell Biol 12:483-90 (2000) DOI:10.1016/S0955-0674(00)00120-4 REFERENCE PMID:10982406 AUTHORS Mullock BM, Smith CW, Ihrke G, Bright NA, Lindsay M, Parkinson EJ, Brooks DA, Parton RG, James DE, Luzio JP, Piper RC. TITLE Syntaxin 7 is localized to late endosome compartments, associates with Vamp 8, and Is required for late endosome-lysosome fusion. JOURNAL Mol Biol Cell 11:3137-53 (2000) DOI:10.1091/mbc.11.9.3137 REFERENCE PMID:9817754 AUTHORS Prekeris R, Klumperman J, Chen YA, Scheller RH. TITLE Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes. JOURNAL J Cell Biol 143:957-71 (1998) DOI:10.1083/jcb.143.4.957 REFERENCE PMID:10564279 AUTHORS Prekeris R, Yang B, Oorschot V, Klumperman J, Scheller RH. TITLE Differential roles of syntaxin 7 and syntaxin 8 in endosomal trafficking. JOURNAL Mol Biol Cell 10:3891-908 (1999) DOI:10.1091/mbc.10.11.3891 REFERENCE PMID:9707576 AUTHORS Sanderfoot AA, Ahmed SU, Marty-Mazars D, Rapoport I, Kirchhausen T, Marty F, Raikhel NV. TITLE A putative vacuolar cargo receptor partially colocalizes with AtPEP12p on a prevacuolar compartment in Arabidopsis roots. JOURNAL Proc Natl Acad Sci U S A 95:9920-5 (1998) DOI:10.1073/pnas.95.17.9920 REFERENCE PMID:11739776 AUTHORS Sanderfoot AA, Kovaleva V, Bassham DC, Raikhel NV. TITLE Interactions between syntaxins identify at least five SNARE complexes within the Golgi/prevacuolar system of the Arabidopsis cell. JOURNAL Mol Biol Cell 12:3733-43 (2001) DOI:10.1091/mbc.12.12.3733 REFERENCE PMID:10557242 AUTHORS Sanderfoot AA, Kovaleva V, Zheng H, Raikhel NV. TITLE The t-SNARE AtVAM3p resides on the prevacuolar compartment in Arabidopsis root cells. JOURNAL Plant Physiol 121:929-38 (1999) DOI:10.1104/pp.121.3.929 REFERENCE PMID:11251103 AUTHORS Sanderfoot AA, Pilgrim M, Adam L, Raikhel NV. TITLE Disruption of individual members of Arabidopsis syntaxin gene families indicates each has essential functions. JOURNAL Plant Cell 13:659-66 (2001) DOI:10.1105/tpc.13.3.659 REFERENCE PMID:9305917 AUTHORS Sato MH, Nakamura N, Ohsumi Y, Kouchi H, Kondo M, Hara-Nishimura I, Nishimura M, Wada Y. TITLE The AtVAM3 encodes a syntaxin-related molecule implicated in the vacuolar assembly in Arabidopsis thaliana. JOURNAL J Biol Chem 272:24530-5 (1997) DOI:10.1074/jbc.272.39.24530 REFERENCE PMID:9710615 AUTHORS Sato TK, Darsow T, Emr SD. TITLE Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking. JOURNAL Mol Cell Biol 18:5308-19 (1998) DOI:10.1128/MCB.18.9.5308 REFERENCE PMID:9813082 AUTHORS Spang A, Schekman R. TITLE Reconstitution of retrograde transport from the Golgi to the ER in vitro. JOURNAL J Cell Biol 143:589-99 (1998) DOI:10.1083/jcb.143.3.589 REFERENCE PMID:10359608 AUTHORS Steegmaier M, Klumperman J, Foletti DL, Yoo JS, Scheller RH. TITLE Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle trafficking. JOURNAL Mol Biol Cell 10:1957-72 (1999) DOI:10.1091/mbc.10.6.1957 REFERENCE PMID:11208143 AUTHORS Steegmaier M, Lee KC, Prekeris R, Scheller RH. TITLE SNARE protein trafficking in polarized MDCK cells. JOURNAL Traffic 1:553-60 (2000) DOI:10.1034/j.1600-0854.2000.010705.x REFERENCE PMID:9852078 AUTHORS Steegmaier M, Yang B, Yoo JS, Huang B, Shen M, Yu S, Luo Y, Scheller RH. TITLE Three novel proteins of the syntaxin/SNAP-25 family. JOURNAL J Biol Chem 273:34171-9 (1998) DOI:10.1074/jbc.273.51.34171 REFERENCE PMID:10683148 AUTHORS Subramaniam VN, Loh E, Horstmann H, Habermann A, Xu Y, Coe J, Griffiths G, Hong W. TITLE Preferential association of syntaxin 8 with the early endosome. JOURNAL J Cell Sci 113 ( Pt 6):997-1008 (2000) REFERENCE PMID:9507000 AUTHORS Tang BL, Tan AE, Lim LK, Lee SS, Low DY, Hong W. TITLE Syntaxin 12, a member of the syntaxin family localized to the endosome. JOURNAL J Biol Chem 273:6944-50 (1998) DOI:10.1074/jbc.273.12.6944 REFERENCE PMID:9628864 AUTHORS Ungermann C, Wickner W. TITLE Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion. JOURNAL EMBO J 17:3269-76 (1998) DOI:10.1093/emboj/17.12.3269 REFERENCE PMID:10036234 AUTHORS Valdez AC, Cabaniols JP, Brown MJ, Roche PA. TITLE Syntaxin 11 is associated with SNAP-23 on late endosomes and the trans-Golgi network. JOURNAL J Cell Sci 112 ( Pt 6):845-54 (1999) REFERENCE PMID:9199167 AUTHORS von Mollard GF, Nothwehr SF, Stevens TH. TITLE The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p. JOURNAL J Cell Biol 137:1511-24 (1997) DOI:10.1083/jcb.137.7.1511 REFERENCE PMID:11278762 AUTHORS Wade N, Bryant NJ, Connolly LM, Simpson RJ, Luzio JP, Piper RC, James DE. TITLE Syntaxin 7 complexes with mouse Vps10p tail interactor 1b, syntaxin 6, vesicle-associated membrane protein (VAMP)8, and VAMP7 in b16 melanoma cells. JOURNAL J Biol Chem 276:19820-7 (2001) DOI:10.1074/jbc.M010838200 REFERENCE PMID:11555414 AUTHORS Wendler F, Tooze S. TITLE Syntaxin 6: the promiscuous behaviour of a SNARE protein. JOURNAL Traffic 2:606-11 (2001) DOI:10.1034/j.1600-0854.2001.20903.x REFERENCE PMID:9614193 AUTHORS Wong SH, Zhang T, Xu Y, Subramaniam VN, Griffiths G, Hong W. TITLE Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with the early endosome. JOURNAL Mol Biol Cell 9:1549-63 (1998) DOI:10.1091/mbc.9.6.1549 REFERENCE PMID:11035026 AUTHORS Xu D, Joglekar AP, Williams AL, Hay JC. TITLE Subunit structure of a mammalian ER/Golgi SNARE complex. JOURNAL J Biol Chem 275:39631-9 (2000) DOI:10.1074/jbc.M007684200 REFERENCE PMID:11323436 AUTHORS Zhang T, Hong W. TITLE Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transport. JOURNAL J Biol Chem 276:27480-7 (2001) DOI:10.1074/jbc.M102786200 REFERENCE PMID:12068098 AUTHORS Zheng H, Bednarek SY, Sanderfoot AA, Alonso J, Ecker JR, Raikhel NV. TITLE NPSN11 is a cell plate-associated SNARE protein that interacts with the syntaxin KNOLLE. JOURNAL Plant Physiol 129:530-9 (2002) DOI:10.1104/pp.003970 REFERENCE PMID:10397763 AUTHORS Zheng H, von Mollard GF, Kovaleva V, Stevens TH, Raikhel NV. TITLE The plant vesicle-associated SNARE AtVTI1a likely mediates vesicle transport from the trans-Golgi network to the prevacuolar compartment. JOURNAL Mol Biol Cell 10:2251-64 (1999) DOI:10.1091/mbc.10.7.2251 KO_PATHWAY ko04130 /// ENTRY map04136 Pathway NAME Autophagy - other DESCRIPTION Autophagy is a degradative pathway for the removal of cytoplasmic materials in eukaryotic cells, and is characterized by the formation of a double-membrane structure called the autophagosome, either in a housekeeping capacity or during stress and senescence. The process of autophagy could be divided into several stages: induction, vesicle nucleation, elongation and closure, and fusion and digestion. Most essential autophagic machineries are conserved throughout eukaryotes (see map04140 for animals and map04138 for fungi). This map is for other eukaryotes including plants and protists, where autophagy related genes (ATGs) play similar roles in the life cycle. However, autophagy has been relatively less studied in lower eukaryotes. CLASS Cellular Processes; Transport and catabolism PATHWAY_MAP map04136 Autophagy - other DBLINKS GO: 0006914 REFERENCE PMID:20962583 AUTHORS Duszenko M, Ginger ML, Brennand A, Gualdron-Lopez M, Colombo MI, Coombs GH, Coppens I, Jayabalasingham B, Langsley G, de Castro SL, Menna-Barreto R, Mottram JC, Navarro M, Rigden DJ, Romano PS, Stoka V, Turk B, Michels PA TITLE Autophagy in protists. JOURNAL Autophagy 7:127-58 (2011) DOI:10.4161/auto.7.2.13310 REFERENCE PMID:21660427 AUTHORS Avin-Wittenberg T, Honig A, Galili G TITLE Variations on a theme: plant autophagy in comparison to yeast and mammals. JOURNAL Protoplasma 249:285-99 (2012) DOI:10.1007/s00709-011-0296-z REFERENCE PMID:22242963 AUTHORS Liu Y, Bassham DC TITLE Autophagy: pathways for self-eating in plant cells. JOURNAL Annu Rev Plant Biol 63:215-37 (2012) DOI:10.1146/annurev-arplant-042811-105441 REFERENCE PMID:22764279 AUTHORS Yoshimoto K TITLE Beginning to understand autophagy, an intracellular self-degradation system in plants. JOURNAL Plant Cell Physiol 53:1355-65 (2012) DOI:10.1093/pcp/pcs099 REFERENCE PMID:24563201 AUTHORS Li F, Chung T, Vierstra RD TITLE AUTOPHAGY-RELATED11 plays a critical role in general autophagy- and senescence-induced mitophagy in Arabidopsis. JOURNAL Plant Cell 26:788-807 (2014) DOI:10.1105/tpc.113.120014 REFERENCE PMID:26598298 AUTHORS Michaeli S, Galili G, Genschik P, Fernie AR, Avin-Wittenberg T TITLE Autophagy in Plants--What's New on the Menu? JOURNAL Trends Plant Sci 21:134-44 (2016) DOI:10.1016/j.tplants.2015.10.008 REFERENCE PMID:26614870 AUTHORS Yang X, Bassham DC TITLE New Insight into the Mechanism and Function of Autophagy in Plant Cells. JOURNAL Int Rev Cell Mol Biol 320:1-40 (2015) DOI:10.1016/bs.ircmb.2015.07.005 KO_PATHWAY ko04136 /// ENTRY map04137 Pathway NAME Mitophagy - animal DESCRIPTION Mitochondria act as the energy powerhouse of the cell, and are essential for eukaryotic cells to grow and function normally. However, deleterious byproducts of oxidative phosphorylation process called reactive oxidative species (ROS) lead to mitochondrial dysfunction. If the damage is too excessive to be repaired, such mitochondria are selectively recognized and targeted for degradation by a specific mode of autophagy, termed mitophagy. The loss of the mitochondrial membrane potential can induce mitophagy, involving the kinase PINK1 and the E3 ligase Parkin. PINK1 serves as the sensor for the mitochondrial depolarization and recruits Parkin, followed by ubiquitin-dependent recruitment of mitophagy receptors. There are also several PINK1/Parkin-independent mitophagy pathways, in which a group of LIR-containing receptors are required in response to different stimuli. Mitophagy contributes to the maintenance of a healthy mitochondrial network and the prevention of programmed cell death. CLASS Cellular Processes; Transport and catabolism PATHWAY_MAP map04137 Mitophagy - animal DBLINKS GO: 0000422 REFERENCE PMID:25611507 AUTHORS Pickrell AM, Youle RJ TITLE The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease. JOURNAL Neuron 85:257-73 (2015) DOI:10.1016/j.neuron.2014.12.007 REFERENCE PMID:25995186 AUTHORS Durcan TM, Fon EA TITLE The three 'P's of mitophagy: PARKIN, PINK1, and post-translational modifications. JOURNAL Genes Dev 29:989-99 (2015) DOI:10.1101/gad.262758.115 REFERENCE PMID:25999423 AUTHORS Shirihai OS, Song M, Dorn GW 2nd TITLE How mitochondrial dynamism orchestrates mitophagy. JOURNAL Circ Res 116:1835-49 (2015) DOI:10.1161/CIRCRESAHA.116.306374 REFERENCE PMID:26611876 AUTHORS Hamacher-Brady A, Brady NR TITLE Mitophagy programs: mechanisms and physiological implications of mitochondrial targeting by autophagy. JOURNAL Cell Mol Life Sci 73:775-95 (2016) DOI:10.1007/s00018-015-2087-8 REFERENCE PMID:26882551 AUTHORS Yamano K, Matsuda N, Tanaka K TITLE The ubiquitin signal and autophagy: an orchestrated dance leading to mitochondrial degradation. JOURNAL EMBO Rep 17:300-16 (2016) DOI:10.15252/embr.201541486 REFERENCE PMID:27021519 AUTHORS Yamaguchi O, Murakawa T, Nishida K, Otsu K TITLE Receptor-mediated mitophagy. JOURNAL J Mol Cell Cardiol 95:50-6 (2016) DOI:10.1016/j.yjmcc.2016.03.010 REFERENCE PMID:27443527 AUTHORS Roberts RF, Tang MY, Fon EA, Durcan TM TITLE Defending the mitochondria: The pathways of mitophagy and mitochondrial-derived vesicles. JOURNAL Int J Biochem Cell Biol 79:427-436 (2016) DOI:10.1016/j.biocel.2016.07.020 REFERENCE PMID:27701735 AUTHORS Arena G, Valente EM TITLE PINK1 in the limelight: multiple functions of an eclectic protein in human health and disease. JOURNAL J Pathol 241:251-263 (2017) DOI:10.1002/path.4815 REL_PATHWAY map04140 Autophagy - animal map04210 Apoptosis KO_PATHWAY ko04137 /// ENTRY map04138 Pathway NAME Autophagy - yeast DESCRIPTION Autophagy is a non-selective and bulk intracellular degradation system of eukaryotic cells and is highly conserved from yeast to human. In this process, the double-membrane vesicle, known as autophagosome, is formed and sequesters organelles or portions of cytosol. The autophagosome is subsequently fused with the vacuole for breakdown by resident hydrolases, and the resulting metabolites are delivered for reuse. In yeast, nutrient withdrawal is the primary stimulus that induces autophagy. Autophagy plays a central role in normal development and cell homeostasis of yeast. CLASS Cellular Processes; Transport and catabolism PATHWAY_MAP map04138 Autophagy - yeast DBLINKS GO: 0006914 REFERENCE PMID:11099404 AUTHORS Klionsky DJ, Emr SD. TITLE Autophagy as a regulated pathway of cellular degradation. JOURNAL Science 290:1717-21 (2000) DOI:10.1126/science.290.5497.1717 REFERENCE PMID:15752997 AUTHORS Thompson AR, Vierstra RD. TITLE Autophagic recycling: lessons from yeast help define the process in plants. JOURNAL Curr Opin Plant Biol 8:165-73 (2005) DOI:10.1016/j.pbi.2005.01.013 REFERENCE PMID:15928708 AUTHORS Lum JJ, DeBerardinis RJ, Thompson CB. TITLE Autophagy in metazoans: cell survival in the land of plenty. JOURNAL Nat Rev Mol Cell Biol 6:439-48 (2005) DOI:10.1038/nrm1660 REFERENCE PMID:15978794 AUTHORS Reggiori F, Klionsky DJ. TITLE Autophagosomes: biogenesis from scratch? JOURNAL Curr Opin Cell Biol 17:415-22 (2005) DOI:10.1016/j.ceb.2005.06.007 REFERENCE PMID:16200202 AUTHORS Levine B, Yuan J. TITLE Autophagy in cell death: an innocent convict? JOURNAL J Clin Invest 115:2679-88 (2005) DOI:10.1172/JCI26390 REFERENCE PMID:19491929 AUTHORS Nakatogawa H, Suzuki K, Kamada Y, Ohsumi Y TITLE Dynamics and diversity in autophagy mechanisms: lessons from yeast. JOURNAL Nat Rev Mol Cell Biol 10:458-67 (2009) DOI:10.1038/nrm2708 REFERENCE PMID:19653858 AUTHORS He C, Klionsky DJ TITLE Regulation mechanisms and signaling pathways of autophagy. JOURNAL Annu Rev Genet 43:67-93 (2009) DOI:10.1146/annurev-genet-102808-114910 REFERENCE PMID:19802558 AUTHORS Yang Z, Klionsky DJ TITLE An overview of the molecular mechanism of autophagy. JOURNAL Curr Top Microbiol Immunol 335:1-32 (2009) DOI:10.1007/978-3-642-00302-8_1 REFERENCE PMID:21187343 AUTHORS Chen Y, Klionsky DJ TITLE The regulation of autophagy - unanswered questions. JOURNAL J Cell Sci 124:161-70 (2011) DOI:10.1242/jcs.064576 REFERENCE PMID:21801009 AUTHORS Mizushima N, Yoshimori T, Ohsumi Y TITLE The role of Atg proteins in autophagosome formation. JOURNAL Annu Rev Cell Dev Biol 27:107-32 (2011) DOI:10.1146/annurev-cellbio-092910-154005 REFERENCE PMID:23733851 AUTHORS Reggiori F, Klionsky DJ TITLE Autophagic processes in yeast: mechanism, machinery and regulation. JOURNAL Genetics 194:341-61 (2013) DOI:10.1534/genetics.112.149013 REFERENCE PMID:24928445 AUTHORS Jin M, Klionsky DJ TITLE Regulation of autophagy: modulation of the size and number of autophagosomes. JOURNAL FEBS Lett 588:2457-63 (2014) DOI:10.1016/j.febslet.2014.06.015 REFERENCE PMID:25948417 AUTHORS Noda NN, Fujioka Y TITLE Atg1 family kinases in autophagy initiation. JOURNAL Cell Mol Life Sci 72:3083-96 (2015) DOI:10.1007/s00018-015-1917-z REL_PATHWAY map04150 mTOR signaling pathway KO_PATHWAY ko04138 /// ENTRY map04139 Pathway NAME Mitophagy - yeast DESCRIPTION Mitophagy, which refers to the selective elimination of impaired or excessive mitochondria, is considered to be the main mechanism for mitochondria quality and quantity control. In yeast, oxidative stress or inhibition of TOR induces expression of Agt32, the indispensable mitochondrial outer membrane receptor. Direct phosphorylation of Atg32 by CK2 triggers mitophagy, and two mitogen-activated protein kinase (MAPK) signal transduction pathways are also important in this process. Atg11 is an adaptor protein for selective autophagy, and recruits the cargo to the phagophore assembly site (PAS), where the autophagosome is generated. Then Atg32-Atg8 interaction enhances the formation of the autophagosome surrounding the mitochondria, which finally fuses with vacuoles for degradation. Atg32-Atg11 interaction may also be regulated by Yme1-mediated processing of Atg32, as well as by mitochondrial fission machinery. Some factors have been suggested to positively or negatively regulate the mitophagy via different mechanisms, including Atg1, Atg33, Mss4, Fmc1, Mdm38, Mip1, and Ubp3-Bre5 deubiquitination complex. CLASS Cellular Processes; Transport and catabolism PATHWAY_MAP map04139 Mitophagy - yeast DBLINKS GO: 0000422 REFERENCE PMID:25603537 AUTHORS Kanki T, Furukawa K, Yamashita S TITLE Mitophagy in yeast: Molecular mechanisms and physiological role. JOURNAL Biochim Biophys Acta 1853:2756-65 (2015) DOI:10.1016/j.bbamcr.2015.01.005 REFERENCE PMID:25753536 AUTHORS Muller M, Lu K, Reichert AS TITLE Mitophagy and mitochondrial dynamics in Saccharomyces cerevisiae. JOURNAL Biochim Biophys Acta 1853:2766-74 (2015) DOI:10.1016/j.bbamcr.2015.02.024 REFERENCE PMID:19619494 AUTHORS Okamoto K, Kondo-Okamoto N, Ohsumi Y TITLE Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy. JOURNAL Dev Cell 17:87-97 (2009) DOI:10.1016/j.devcel.2009.06.013 REFERENCE PMID:19619495 AUTHORS Kanki T, Wang K, Cao Y, Baba M, Klionsky DJ TITLE Atg32 is a mitochondrial protein that confers selectivity during mitophagy. JOURNAL Dev Cell 17:98-109 (2009) DOI:10.1016/j.devcel.2009.06.014 REFERENCE PMID:21576396 AUTHORS Mao K, Wang K, Zhao M, Xu T, Klionsky DJ TITLE Two MAPK-signaling pathways are required for mitophagy in Saccharomyces cerevisiae. JOURNAL J Cell Biol 193:755-67 (2011) DOI:10.1083/jcb.201102092 REFERENCE PMID:21757540 AUTHORS Aoki Y, Kanki T, Hirota Y, Kurihara Y, Saigusa T, Uchiumi T, Kang D TITLE Phosphorylation of Serine 114 on Atg32 mediates mitophagy. JOURNAL Mol Biol Cell 22:3206-17 (2011) DOI:10.1091/mbc.E11-02-0145 REFERENCE PMID:23897086 AUTHORS Kanki T, Kurihara Y, Jin X, Goda T, Ono Y, Aihara M, Hirota Y, Saigusa T, Aoki Y, Uchiumi T, Kang D TITLE Casein kinase 2 is essential for mitophagy. JOURNAL EMBO Rep 14:788-94 (2013) DOI:10.1038/embor.2013.114 REFERENCE PMID:22308029 AUTHORS Kondo-Okamoto N, Noda NN, Suzuki SW, Nakatogawa H, Takahashi I, Matsunami M, Hashimoto A, Inagaki F, Ohsumi Y, Okamoto K TITLE Autophagy-related protein 32 acts as autophagic degron and directly initiates mitophagy. JOURNAL J Biol Chem 287:10631-8 (2012) DOI:10.1074/jbc.M111.299917 REFERENCE PMID:23810512 AUTHORS Mao K, Wang K, Liu X, Klionsky DJ TITLE The scaffold protein Atg11 recruits fission machinery to drive selective mitochondria degradation by autophagy. JOURNAL Dev Cell 26:9-18 (2013) DOI:10.1016/j.devcel.2013.05.024 REFERENCE PMID:24025448 AUTHORS Wang K, Jin M, Liu X, Klionsky DJ TITLE Proteolytic processing of Atg32 by the mitochondrial i-AAA protease Yme1 regulates mitophagy. JOURNAL Autophagy 9:1828-36 (2013) DOI:10.4161/auto.26281 REFERENCE PMID:17166847 AUTHORS Tal R, Winter G, Ecker N, Klionsky DJ, Abeliovich H TITLE Aup1p, a yeast mitochondrial protein phosphatase homolog, is required for efficient stationary phase mitophagy and cell survival. JOURNAL J Biol Chem 282:5617-24 (2007) DOI:10.1074/jbc.M605940200 REFERENCE PMID:19793921 AUTHORS Kanki T, Wang K, Baba M, Bartholomew CR, Lynch-Day MA, Du Z, Geng J, Mao K, Yang Z, Yen WL, Klionsky DJ TITLE A genomic screen for yeast mutants defective in selective mitochondria autophagy. JOURNAL Mol Biol Cell 20:4730-8 (2009) DOI:10.1091/mbc.E09-03-0225 REFERENCE PMID:22977244 AUTHORS Wang K, Yang Z, Liu X, Mao K, Nair U, Klionsky DJ TITLE Phosphatidylinositol 4-kinases are required for autophagic membrane trafficking. JOURNAL J Biol Chem 287:37964-72 (2012) DOI:10.1074/jbc.M112.371591 REFERENCE PMID:15947785 AUTHORS Priault M, Salin B, Schaeffer J, Vallette FM, di Rago JP, Martinou JC TITLE Impairing the bioenergetic status and the biogenesis of mitochondria triggers mitophagy in yeast. JOURNAL Cell Death Differ 12:1613-21 (2005) DOI:10.1038/sj.cdd.4401697 REFERENCE PMID:17541427 AUTHORS Nowikovsky K, Reipert S, Devenish RJ, Schweyen RJ TITLE Mdm38 protein depletion causes loss of mitochondrial K+/H+ exchange activity, osmotic swelling and mitophagy. JOURNAL Cell Death Differ 14:1647-56 (2007) DOI:10.1038/sj.cdd.4402167 REFERENCE PMID:17404498 AUTHORS Zhang Y, Qi H, Taylor R, Xu W, Liu LF, Jin S TITLE The role of autophagy in mitochondria maintenance: characterization of mitochondrial functions in autophagy-deficient S. cerevisiae strains. JOURNAL Autophagy 3:337-46 (2007) DOI:10.4161/auto.4127 REFERENCE PMID:25704822 AUTHORS Muller M, Kotter P, Behrendt C, Walter E, Scheckhuber CQ, Entian KD, Reichert AS TITLE Synthetic quantitative array technology identifies the Ubp3-Bre5 deubiquitinase complex as a negative regulator of mitophagy. JOURNAL Cell Rep 10:1215-25 (2015) DOI:10.1016/j.celrep.2015.01.044 REL_PATHWAY map04011 MAPK signaling pathway - yeast map04138 Autophagy - yeast KO_PATHWAY ko04139 /// ENTRY map00121 Pathway NAME Secondary bile acid biosynthesis DESCRIPTION The secondary bile acids are derived from the primary bile acids by the enzymatic action of intestinal bacteria through the process of deconjugation and dehydroxylation. The secondary bile acids in humans include deoxycholic acid and lithocholic acid, formed from the 7alpha-dehydroxylation of cholic acid and chenodeoxycholic acid, respectively. CLASS Metabolism; Lipid metabolism PATHWAY_MAP map00121 Secondary bile acid biosynthesis REFERENCE PMID:18488143 AUTHORS Hofmann AF, Hagey LR TITLE Bile acids: chemistry, pathochemistry, biology, pathobiology, and therapeutics. JOURNAL Cell Mol Life Sci 65:2461-83 (2008) DOI:10.1007/s00018-008-7568-6 REFERENCE PMID:16299351 AUTHORS Ridlon JM, Kang DJ, Hylemon PB TITLE Bile salt biotransformations by human intestinal bacteria. JOURNAL J Lipid Res 47:241-59 (2006) DOI:10.1194/jlr.R500013-JLR200 REFERENCE PMID:19464381 AUTHORS Ridlon JM, Kang DJ, Hylemon PB TITLE Isolation and characterization of a bile acid inducible 7alpha-dehydroxylating operon in Clostridium hylemonae TN271. JOURNAL Anaerobe 16:137-46 (2010) DOI:10.1016/j.anaerobe.2009.05.004 REFERENCE PMID:18047844 AUTHORS Kang DJ, Ridlon JM, Moore DR 2nd, Barnes S, Hylemon PB TITLE Clostridium scindens baiCD and baiH genes encode stereo-specific 7alpha/7beta-hydroxy-3-oxo-delta4-cholenoic acid oxidoreductases. JOURNAL Biochim Biophys Acta 1781:16-25 (2008) DOI:10.1016/j.bbalip.2007.10.008 REFERENCE PMID:16061950 AUTHORS Moschetta A, Xu F, Hagey LR, van Berge-Henegouwen GP, van Erpecum KJ, Brouwers JF, Cohen JC, Bierman M, Hobbs HH, Steinbach JH, Hofmann AF TITLE A phylogenetic survey of biliary lipids in vertebrates. JOURNAL J Lipid Res 46:2221-32 (2005) DOI:10.1194/jlr.M500178-JLR200 REL_PATHWAY map00120 Primary bile acid biosynthesis KO_PATHWAY ko00121 /// ENTRY map00120 Pathway NAME Primary bile acid biosynthesis DESCRIPTION Bile acids are steroid carboxylic acids derived from cholesterol in vertebrates. The primary bile acids, cholic acid and chenodeoxycholic acid, are synthesized in the liver and conjugated with taurine or glycine before secretion via bile into the intestine. The conversion from cholesterol to cholic and chenodeoxycholic acids involves four steps: 1) the initiation of synthesis by 7alpha-hydroxylation of sterol precursors, 2) further modifications to the ring structures, 3) side-chain oxidation and shortening (cleavage) by three carbons, and 4) conjugation of the bile acid with taurine or glycine. CLASS Metabolism; Lipid metabolism PATHWAY_MAP map00120 Primary bile acid biosynthesis MODULE M00104 Bile acid biosynthesis, cholesterol => cholate/chenodeoxycholate [PATH:map00120] M00106 Conjugated bile acid biosynthesis, cholate => taurocholate/glycocholate [PATH:map00120] M00862 beta-Oxidation, peroxisome, tri/dihydroxycholestanoyl-CoA => choloyl/chenodeoxycholoyl-CoA [PATH:map00120] REFERENCE PMID:12543708 AUTHORS Russell DW TITLE The enzymes, regulation, and genetics of bile acid synthesis. JOURNAL Annu Rev Biochem 72:137-74 (2003) DOI:10.1146/annurev.biochem.72.121801.161712 REFERENCE PMID:17346171 AUTHORS Norlin M, Wikvall K TITLE Enzymes in the conversion of cholesterol into bile acids. JOURNAL Curr Mol Med 7:199-218 (2007) DOI:10.2174/156652407780059168 REFERENCE PMID:10198776 AUTHORS Vlahcevic ZR, Pandak WM, Stravitz RT TITLE Regulation of bile acid biosynthesis. JOURNAL Gastroenterol Clin North Am 28:1-25, v (1999) DOI:10.1016/S0889-8553(05)70041-8 REFERENCE PMID:18081658 AUTHORS Pellicoro A, Faber KN TITLE Review article: The function and regulation of proteins involved in bile salt biosynthesis and transport. JOURNAL Aliment Pharmacol Ther 26 Suppl 2:149-60 (2007) DOI:10.1111/j.1365-2036.2007.03522.x REFERENCE PMID:18488143 AUTHORS Hofmann AF, Hagey LR TITLE Bile acids: chemistry, pathochemistry, biology, pathobiology, and therapeutics. JOURNAL Cell Mol Life Sci 65:2461-83 (2008) DOI:10.1007/s00018-008-7568-6 REFERENCE PMID:11067870 AUTHORS Schwarz M, Wright AC, Davis DL, Nazer H, Bjorkhem I, Russell DW TITLE The bile acid synthetic gene 3beta-hydroxy-Delta(5)-C(27)-steroid oxidoreductase is mutated in progressive intrahepatic cholestasis. JOURNAL J Clin Invest 106:1175-84 (2000) DOI:10.1172/JCI10902 REFERENCE PMID:16299351 AUTHORS Ridlon JM, Kang DJ, Hylemon PB TITLE Bile salt biotransformations by human intestinal bacteria. JOURNAL J Lipid Res 47:241-59 (2006) DOI:10.1194/jlr.R500013-JLR200 REFERENCE PMID:9292932 AUTHORS Bortolini O, Medici A, Poli S TITLE Biotransformations on steroid nucleus of bile acids. JOURNAL Steroids 62:564-77 (1997) DOI:10.1016/S0039-128X(97)00043-3 REL_PATHWAY map00100 Steroid biosynthesis map00121 Secondary bile acid biosynthesis KO_PATHWAY ko00120 /// ENTRY map07230 Drug Pathway NAME GABA-A receptor agonists/antagonists PATHWAY_MAP map07230 GABA-A receptor agonists/antagonists COMPOUND C07521 Thiopental C09364 Bicuculline C09529 Picrotoxinin D00225 Alprazolam (JP19/USP/INN) D00267 Chlordiazepoxide (JP19/USP/INN) D00280 Clonazepam (JP19/USP/INN) D00293 Diazepam (JP19/USP/INN) D00311 Estazolam (JP19/USP/INN) D00329 Flurazepam (JAN/INN) D00365 Lorazepam (JP19/USP/INN) D00370 Temazepam (USP/INN) D00387 Triazolam (JP19/USP/INN) D00430 Secobarbital (USP/INN) D00457 Quazepam (JAN/USP/INN) D00464 Oxazepam (JAN/USP/INN) D00470 Prazepam (JP19/USAN/INN) D00474 Primidone (JP19/USP/INN) D00499 Pentobarbital (USP/INN) D00500 Pentobarbital sodium (JAN/USP) D00506 Phenobarbital (JP19/USP/INN) D00531 Nitrazepam (JP19/USAN/INN) D00549 Propofol (JAN/USP/INN) D00550 Midazolam (JAN/USP/INN) D00555 Amobarbital (JP19/INN) D00693 Chlordiazepoxide hydrochloride (JAN/USP) D00694 Clorazepate dipotassium (JP19/USP) D00695 Flurazepam hydrochloride (USP) D00696 Midazolam hydrochloride (USAN) D00697 Flumazenil (JAN/USP/INN) D00700 Mephobarbital (JAN/USP) D00701 Phenobarbital sodium (JAN/USP/INN) D00706 Zolpidem tartrate (JP19/USP) D00713 Thiamylal sodium (JP19) D00714 Thiopental sodium (JP19/USP/INN) D01071 Hexobarbital (JAN/INN) D01230 Flunitrazepam (JP19/USAN/INN) D01245 Bromazepam (JP19/USAN/INN) D01254 Tofisopam (JP19/INN) D01268 Cloxazolam (JP19/INN) D01278 Oxazolam (JP19/INN) D01279 Flutoprazepam (JAN/INN) D01286 Flutazolam (JAN/INN) D01292 Medazepam (JP19/INN) D01293 Ethyl loflazepate (JP19/INN) D01310 Secobarbital sodium (JAN/USP) D01316 Mexazolam (JAN/INN) D01328 Clotiazepam (JP19/INN) D01354 Fludiazepam (JP19/INN) D01372 Zopiclone (JP19/INN) D01408 Flurazepam hydrochloride (JP19) D01514 Etizolam (JP19/INN) D01564 Rilmazafone hydrochloride hydrate (JP19) D01593 Nimetazepam (JAN/INN) D01657 Lormetazepam (JAN/USAN/INN) D01740 Barbital (JP19/INN) D01744 Brotizolam (JP19/USAN/INN) D01758 Haloxazolam (JP19/INN) D02252 Amobarbital sodium (JAN/USP) D02253 Pentobarbital calcium (JP19) D02618 Butobarbital (BAN) D02624 Eszopiclone (JAN/USP/INN) D03562 Clorazepate monopotassium (USAN) D04257 Fospropofol disodium (USAN) D04882 Medazepam hydrochloride (USAN) D05028 Midazolam maleate (USAN) D06106 Thiamylal D07409 Pentetrazol (INN) D08356 Phenobarbital diethylamine D08481 Rilmazafone (INN) D08690 Zolpidem (INN) /// ENTRY map07231 Drug Pathway NAME Sodium channel blocking drugs PATHWAY_MAP map07231 Sodium channel blocking drugs COMPOUND D00110 Cocaine (USP) D00199 Ajmaline (JP19) D00252 Carbamazepine (JP19/USP/INN) D00303 Disopyramide (JP19/USAN/INN) D00354 Lamotrigine (JAN/USP/INN) D00358 Lidocaine (JP19/USP/INN) D00477 Procainamide hydrochloride (JP19/USP) D00512 Phenytoin (JP19/USP/INN) D00537 Topiramate (JAN/USP/INN) D00538 Zonisamide (JP19/USP/INN) D00551 Tetracaine (USP/INN) D00552 Benzocaine (USP/INN) D00553 Prilocaine (USP/INN) D00631 Bepridil hydrochloride (USAN) D00636 Amiodarone hydrochloride (JP19/USP) D00637 Disopyramide phosphate (JAN/USP) D00638 Flecainide acetate (JP19/USP) D00639 Mexiletine hydrochloride (JP19/USP) D00640 Propafenone hydrochloride (JP19/USP) D00642 Quinidine gluconate (USP) D00643 Quinidine polygalacturonate D00733 Dibucaine (USP) D00738 Mepivacaine hydrochloride (JP19/USP) D00740 Procaine hydrochloride (JP19/USP) D00741 Tetracaine hydrochloride (JP19/USP) D01287 Levobupivacaine hydrochloride (JAN/USAN) D01326 Aprindine hydrochloride (JP19/USAN) D01450 Bupivacaine hydrochloride (USP) D01455 Cifenline succinate (USAN) D01479 Ambroxol hydrochloride (JAN) D01554 Pilsicainide hydrochloride hydrate (JP19) D01785 Pirmenol hydrochloride hydrate (JAN) D02086 Lidocaine hydrochloride (JAN/USP) D02088 Tocainide hydrochloride (USP) D02098 Proparacaine hydrochloride (USP) D02103 Phenytoin sodium (USP) D02182 Cocaine hydrochloride (JP19/USP) D02220 Dibucaine hydrochloride (JP19/USP) D02272 Quinidine sulfate (USP) D02537 Dronedarone (INN) D02910 Amiodarone (USAN/INN) D02969 Aprindine (USAN/INN) D03492 Cifenline (USAN) D03914 Dronedarone hydrochloride (USP) D04048 Ropivacaine hydrochloride (USP) D06172 Tocainide (USAN/INN) D06517 Pirmenol hydrochloride (USAN) D07442 Ambroxol (INN) D07520 Bepridil (INN) D07552 Bupivacaine (USAN/INN) D07595 Fosphenytoin sodium hydrate (JAN) D07962 Flecainide (INN) D07993 Fosphenytoin (INN) D08116 Levobupivacaine (INN) D08127 Lidocaine hydrochloride monohydrate D08181 Mepivacaine (INN) D08215 Mexiletine (INN) D08377 Pilsicainide (INN) D08394 Pirmenol (INN) D08421 Procainamide (INN) D08422 Procaine (INN) D08435 Propafenone (INN) D08448 Proxymetacaine (INN) D08458 Quinidine (BAN) D08459 Quinidine phenylethylbarbiturate D08490 Ropivacaine (INN) REL_PATHWAY map07037 Antiarrhythmic drugs /// ENTRY C00099 Compound NAME beta-Alanine; 3-Aminopropionic acid; 3-Aminopropanoate FORMULA C3H7NO2 EXACT_MASS 89.0477 MOL_WEIGHT 89.09 REMARK Same as: D07561 REACTION R00489 R00904 R00905 R00906 R00907 R00908 R00909 R00910 R00911 R00912 R00913 R00914 R00915 R00916 R00917 R01164 R01166 R02473 R02474 R02741 R03286 R03288 R03935 R09379 R09648 R10821 PATHWAY map00240 Pyrimidine metabolism map00410 beta-Alanine metabolism map00640 Propanoate metabolism map00770 Pantothenate and CoA biosynthesis map01100 Metabolic pathways map01110 Biosynthesis of secondary metabolites map01240 Biosynthesis of cofactors map04080 Neuroactive ligand-receptor interaction map04974 Protein digestion and absorption MODULE M00046 Pyrimidine degradation, uracil => beta-alanine, thymine => 3-aminoisobutanoate M00119 Pantothenate biosynthesis, valine/L-aspartate => pantothenate M00913 Pantothenate biosynthesis, 2-oxoisovalerate/spermine => pantothenate ENZYME 1.2.1.3 1.2.1.5 1.2.1.19 1.5.1.26 2.6.1.18 2.6.1.19 2.6.1.55 2.6.1.120 2.8.3.- 3.4.13.4 3.4.13.5 3.4.13.18 3.4.13.20 3.5.1.6 3.5.1.21 3.5.1.22 3.5.1.100 3.5.3.17 4.1.1.11 4.1.1.15 6.3.2.1 6.3.2.11 6.3.2.23 6.3.2.36 6.3.2.44 BRITE Compounds with biological roles [BR:br08001] Peptides Amino acids Other amino acids C00099 beta-Alanine Amines Biogenic amines C00099 beta-Alanine DBLINKS CAS: 107-95-9 PubChem: 3399 ChEBI: 16958 KNApSAcK: C00001333 PDB-CCD: BAL J-GLOBAL: J4.070C ATOM 6 1 C1b C 25.6778 -16.8919 2 C6a C 24.4732 -16.1936 3 C1b C 26.8940 -16.1936 4 O6a O 23.2571 -16.8978 5 O6a O 24.4732 -14.7912 6 N1a N 28.1045 -16.8919 BOND 5 1 1 2 1 2 1 3 1 3 2 4 1 4 2 5 2 5 3 6 1 ///